Structures of Actinonin-bound Peptide Deformylases from Enterococcus faecalis and Streptococcus pyogenes

Title
Structures of Actinonin-bound Peptide Deformylases from Enterococcus faecalis and Streptococcus pyogenes
Authors
김국한이원규최경재김은경
Keywords
actinonin; antibacterial target; drug design; Enterococcus faecalis; peptide deformylase; Streptococcus pyogenes
Issue Date
2014-10
Publisher
한국응용생명화학회지; JOURNAL OF THE KOREAN SOCIETY FOR APPLIED BIOLOGICAL CHEMISTRY
Citation
VOL 57, NO 5, 565-571
Abstract
Bacterial resistance to many existing antibiotics is a growing health concern worldwide. There is an urgent need to identify new antibiotics with unexploited modes of action. Peptide deformylase (PDF) is an essential enzyme involved in N-terminal protein processing in eubacteria but not in higher organisms. Therefore, PDF is considered an attractive target for the development of novel antibiotics. Here, we report the structures of the PDFs from Enterococcus faecalis (EfPDF) and Streptococcus pyogenes (SpyPDF) complexed with actinonin at 1.4 and 2.1 Å resolutions, respectively. Actinonin, a naturally occurring, highly potent inhibitor, is bound tightly at the active site. The conformation of actinonin in the EfPDF and SpyPDF complexes was similar to those of all others. The detailed information from this study will facilitate the development of novel antibacterial molecules.
URI
http://pubs.kist.re.kr/handle/201004/48581
ISSN
17382203
Appears in Collections:
KIST Publication > Article
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